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Conserved domains on  [gi|970471527|ref|WP_058750509|]
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ATP-dependent zinc metalloprotease FtsH [Curtobacterium oceanosedimentum]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 11422021)

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein such as ATP-dependent zinc metalloprotease FtsH, which targets both cytoplasmic and membrane proteins and plays a role in quality control of integral membrane proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
15-603 0e+00

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1022.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  15 LIALVGIFIGWSVIAQSGTQQIDTQKGLEQLADGKVSSVVVnsTEQRVDLTLKDGnAKEQFYYSTPRGEEVIKAVNDANL 94
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTI--QGDRITGTLKDG-TKTRFTTYRVNDPELVDLLEEKGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  95 PdgYN-DTVQQGNWFLSLLGIILPFLIIGALFWFLLSSAQGGGSKVMQFGKSRAKMNNKENPQVSFADVAGSDEAIEELH 173
Cdd:COG0465   78 E--VTaKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 174 EIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQNAP 253
Cdd:COG0465  156 EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 254 AIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGVDAPSLG 333
Cdd:COG0465  236 CIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 334 GRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDEAVDRVMAGPQRRTRIMSD 413
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 414 QEKLITAYHEGGHALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYSVTRNELLDQLTYAMGGRVAEEIVFHDPTT 493
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTT 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 494 GASNDIEKATSTARKMVTEYGMSRAVGSVKLGSGSSEPFVGREMggGSGRDYSENIAETVDAETRALLEAAHDEAYQVLN 573
Cdd:COG0465  476 GASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDI--GQSRNYSEETAREIDEEVRRIIDEAYERAKEILT 553
                        570       580       590
                 ....*....|....*....|....*....|
gi 970471527 574 DNRDILDRLAGELLEKETLDAPELVEIFKD 603
Cdd:COG0465  554 ENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
15-603 0e+00

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1022.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  15 LIALVGIFIGWSVIAQSGTQQIDTQKGLEQLADGKVSSVVVnsTEQRVDLTLKDGnAKEQFYYSTPRGEEVIKAVNDANL 94
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTI--QGDRITGTLKDG-TKTRFTTYRVNDPELVDLLEEKGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  95 PdgYN-DTVQQGNWFLSLLGIILPFLIIGALFWFLLSSAQGGGSKVMQFGKSRAKMNNKENPQVSFADVAGSDEAIEELH 173
Cdd:COG0465   78 E--VTaKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 174 EIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQNAP 253
Cdd:COG0465  156 EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 254 AIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGVDAPSLG 333
Cdd:COG0465  236 CIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 334 GRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDEAVDRVMAGPQRRTRIMSD 413
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 414 QEKLITAYHEGGHALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYSVTRNELLDQLTYAMGGRVAEEIVFHDPTT 493
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTT 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 494 GASNDIEKATSTARKMVTEYGMSRAVGSVKLGSGSSEPFVGREMggGSGRDYSENIAETVDAETRALLEAAHDEAYQVLN 573
Cdd:COG0465  476 GASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDI--GQSRNYSEETAREIDEEVRRIIDEAYERAKEILT 553
                        570       580       590
                 ....*....|....*....|....*....|
gi 970471527 574 DNRDILDRLAGELLEKETLDAPELVEIFKD 603
Cdd:COG0465  554 ENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
106-602 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 815.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  106 NWFLSLLGIILPFLIIGALFWFLLSSAQGGGSKVMQFGKSRAKMNNKENPQVSFADVAGSDEAIEELHEIKEFLQEPAKF 185
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  186 QAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVG 265
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  266 RHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKG 345
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  346 KPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDEAVDRVMAGPQRRTRIMSDQEKLITAYHEGG 425
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  426 HALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYSVTRNELLDQLTYAMGGRVAEEIVFHDPTTGASNDIEKATST 505
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  506 ARKMVTEYGMSRAVGSVKLGSGSSEPFVGREMggGSGRDYSENIAETVDAETRALLEAAHDEAYQVLNDNRDILDRLAGE 585
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGF--AKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKA 478
                         490
                  ....*....|....*..
gi 970471527  586 LLEKETLDAPELVEIFK 602
Cdd:TIGR01241 479 LLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
12-616 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 647.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  12 LYVLIALVGIFIGWSVIAQSGTQQIDTQKGLEQLADGKVSSVV-----VNSTE----QRVDLTLKDGNAKEQFyySTP-- 80
Cdd:CHL00176  10 LISLPLIVEKFTVWDVFYYSSVEDGLKSPNNPDVVQNKASSRMtygrfLEYLDmgwiKKVDLYDNGRTAIVEA--SSPel 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  81 -------------RGEEVIKAVNDANLPDGYNDTVQQGNWFLSLLGIILPFLIIGALFWFL-LSSAQGGGSK--VMQFGK 144
Cdd:CHL00176  88 gnrpqrirvelpvGASELIQKLKEANIDFDAHPPVLKSNIVTILSNLLLPLILIGVLWFFFqRSSNFKGGPGqnLMNFGK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 145 SRAKMNNKENPQVSFADVAGSDEAIEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSI 224
Cdd:CHL00176 168 SKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 225 SGSDFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAA 304
Cdd:CHL00176 248 SGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAA 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 305 TNRPDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSN 384
Cdd:CHL00176 328 TNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRK 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 385 AQLIDNRALDEAVDRVMAGPQRRTRIMSDQEKLItAYHEGGHALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYS 464
Cdd:CHL00176 408 KATITMKEIDTAIDRVIAGLEGTPLEDSKNKRLI-AYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSL 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 465 VTRNELLDQLTYAMGGRVAEEIVFHDP--TTGASNDIEKATSTARKMVTEYGMSrAVGSVKL-GSGSSEPFVGREMGGGS 541
Cdd:CHL00176 487 VSRSQILARIVGALGGRAAEEVVFGSTevTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLeSNNSTDPFLGRFMQRNS 565
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970471527 542 grDYSENIAETVDAETRALLEAAHDEAYQVLNDNRDILDRLAGELLEKETLDAPELVEIFKDVRKLPERPQWLSS 616
Cdd:CHL00176 566 --EYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTILPPKKTWKAW 638
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
157-327 8.43e-122

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 358.85  E-value: 8.43e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 157 VSFADVAGSDEAIEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGV 236
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 237 GASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALL 316
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 970471527 317 RPGRFDRQIGV 327
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
409-600 3.83e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 272.94  E-value: 3.83e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  409 RIMSDQEKLITAYHEGGHALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYSVTRNELLDQLTYAMGGRVAEEIVF 488
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  489 HDPTTGASNDIEKATSTARKMVTEYGMSRAVGSVKLGSGSSEPFVGREMggGSGRDYSENIAETVDAETRALLEAAHDEA 568
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGM--GKRKPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 970471527  569 YQVLNDNRDILDRLAGELLEKETLDAPELVEI 600
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
193-330 4.37e-20

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 87.04  E-value: 4.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527   193 PKGVLLYGPPGTGKTLLARAVAGEA---GVPFYSISGSDFVE--------------MFVGVGASRVRDLFEQAKQNAPAI 255
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970471527   256 VFIDEIDAVGRHRGagigggndEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPgRFDRQIGVDAP 330
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
15-603 0e+00

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1022.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  15 LIALVGIFIGWSVIAQSGTQQIDTQKGLEQLADGKVSSVVVnsTEQRVDLTLKDGnAKEQFYYSTPRGEEVIKAVNDANL 94
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTI--QGDRITGTLKDG-TKTRFTTYRVNDPELVDLLEEKGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  95 PdgYN-DTVQQGNWFLSLLGIILPFLIIGALFWFLLSSAQGGGSKVMQFGKSRAKMNNKENPQVSFADVAGSDEAIEELH 173
Cdd:COG0465   78 E--VTaKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 174 EIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQNAP 253
Cdd:COG0465  156 EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 254 AIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGVDAPSLG 333
Cdd:COG0465  236 CIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 334 GRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDEAVDRVMAGPQRRTRIMSD 413
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 414 QEKLITAYHEGGHALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYSVTRNELLDQLTYAMGGRVAEEIVFHDPTT 493
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTT 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 494 GASNDIEKATSTARKMVTEYGMSRAVGSVKLGSGSSEPFVGREMggGSGRDYSENIAETVDAETRALLEAAHDEAYQVLN 573
Cdd:COG0465  476 GASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDI--GQSRNYSEETAREIDEEVRRIIDEAYERAKEILT 553
                        570       580       590
                 ....*....|....*....|....*....|
gi 970471527 574 DNRDILDRLAGELLEKETLDAPELVEIFKD 603
Cdd:COG0465  554 ENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
106-602 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 815.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  106 NWFLSLLGIILPFLIIGALFWFLLSSAQGGGSKVMQFGKSRAKMNNKENPQVSFADVAGSDEAIEELHEIKEFLQEPAKF 185
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  186 QAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVG 265
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  266 RHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKG 345
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  346 KPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDEAVDRVMAGPQRRTRIMSDQEKLITAYHEGG 425
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  426 HALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYSVTRNELLDQLTYAMGGRVAEEIVFHDPTTGASNDIEKATST 505
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  506 ARKMVTEYGMSRAVGSVKLGSGSSEPFVGREMggGSGRDYSENIAETVDAETRALLEAAHDEAYQVLNDNRDILDRLAGE 585
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGF--AKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKA 478
                         490
                  ....*....|....*..
gi 970471527  586 LLEKETLDAPELVEIFK 602
Cdd:TIGR01241 479 LLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
12-616 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 647.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  12 LYVLIALVGIFIGWSVIAQSGTQQIDTQKGLEQLADGKVSSVV-----VNSTE----QRVDLTLKDGNAKEQFyySTP-- 80
Cdd:CHL00176  10 LISLPLIVEKFTVWDVFYYSSVEDGLKSPNNPDVVQNKASSRMtygrfLEYLDmgwiKKVDLYDNGRTAIVEA--SSPel 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  81 -------------RGEEVIKAVNDANLPDGYNDTVQQGNWFLSLLGIILPFLIIGALFWFL-LSSAQGGGSK--VMQFGK 144
Cdd:CHL00176  88 gnrpqrirvelpvGASELIQKLKEANIDFDAHPPVLKSNIVTILSNLLLPLILIGVLWFFFqRSSNFKGGPGqnLMNFGK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 145 SRAKMNNKENPQVSFADVAGSDEAIEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSI 224
Cdd:CHL00176 168 SKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 225 SGSDFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAA 304
Cdd:CHL00176 248 SGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAA 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 305 TNRPDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSN 384
Cdd:CHL00176 328 TNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRK 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 385 AQLIDNRALDEAVDRVMAGPQRRTRIMSDQEKLItAYHEGGHALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYS 464
Cdd:CHL00176 408 KATITMKEIDTAIDRVIAGLEGTPLEDSKNKRLI-AYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSL 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 465 VTRNELLDQLTYAMGGRVAEEIVFHDP--TTGASNDIEKATSTARKMVTEYGMSrAVGSVKL-GSGSSEPFVGREMGGGS 541
Cdd:CHL00176 487 VSRSQILARIVGALGGRAAEEVVFGSTevTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLeSNNSTDPFLGRFMQRNS 565
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970471527 542 grDYSENIAETVDAETRALLEAAHDEAYQVLNDNRDILDRLAGELLEKETLDAPELVEIFKDVRKLPERPQWLSS 616
Cdd:CHL00176 566 --EYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTILPPKKTWKAW 638
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
11-605 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 572.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  11 YLYVLIALVGIFIGWSViAQSGTQQIDTQKGLEQLADGKVSSVVVNSTEqrVDLTLKDGNAKEQFYystprgeevikAVN 90
Cdd:PRK10733   8 WLVIAVVLMSVFQSFGP-SESNGRKVDYSTFLQEVNQDQVREARINGRE--INVTKKDSNRYTTYI-----------PVN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  91 DANLPDGY--------NDTVQQGNWFLSLLGIILPFLIIGALFWFLLSSAQGGGSK-VMQFGKSRAKMNNKENPQVSFAD 161
Cdd:PRK10733  74 DPKLLDNLltknvkvvGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKgAMSFGKSKARMLTEDQIKTTFAD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 162 VAGSDEAIEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRV 241
Cdd:PRK10733 154 VAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 242 RDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRF 321
Cdd:PRK10733 234 RDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRF 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 322 DRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDEAVDRVM 401
Cdd:PRK10733 314 DRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIM 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 402 AGPQRRTRIMSDQEKLITAYHEGGHALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYSVTRNELLDQLTYAMGGR 481
Cdd:PRK10733 394 MGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGR 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 482 VAEEIVF--HDPTTGASNDIEKATSTARKMVTEYGMSRAVGSVKLGSGSSEPFVGREMggGSGRDYSENIAETVDAETRA 559
Cdd:PRK10733 474 LAEEIIYgpEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSV--AKAKHMSDETARIIDQEVKA 551
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 970471527 560 LLEAAHDEAYQVLNDNRDILDRLAGELLEKETLDAPELVEIF--KDVR 605
Cdd:PRK10733 552 LIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMarRDVR 599
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
157-327 8.43e-122

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 358.85  E-value: 8.43e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 157 VSFADVAGSDEAIEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGV 236
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 237 GASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALL 316
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 970471527 317 RPGRFDRQIGV 327
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
141-409 2.89e-113

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 343.14  E-value: 2.89e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 141 QFGKSRAKMNNKENPQVSFADVAGSDEAIEELHE-IKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGV 219
Cdd:COG1222   59 RLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREaVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGA 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 220 PFYSISGSDFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGndEREQTLNQLLVEMDGFDGKTNV 299
Cdd:COG1222  139 PFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDV 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 300 ILIAATNRPDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALL 379
Cdd:COG1222  217 LIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMF 296
                        250       260       270
                 ....*....|....*....|....*....|
gi 970471527 380 TARSNAQLIDNRALDEAVDRVMAGPQRRTR 409
Cdd:COG1222  297 AIREGRDTVTMEDLEKAIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
153-407 8.41e-99

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 307.91  E-value: 8.41e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 153 ENPQVSFADVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVE 231
Cdd:PRK03992 124 ESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQ 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 232 MFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVL 311
Cdd:PRK03992 204 KFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDIL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 312 DPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNR 391
Cdd:PRK03992 284 DPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTME 363
                        250
                 ....*....|....*.
gi 970471527 392 ALDEAVDRVMAGPQRR 407
Cdd:PRK03992 364 DFLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
409-600 3.83e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 272.94  E-value: 3.83e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  409 RIMSDQEKLITAYHEGGHALAAAAMRHTDPVTKITILPRGRALGYTMVLPLEDKYSVTRNELLDQLTYAMGGRVAEEIVF 488
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  489 HDPTTGASNDIEKATSTARKMVTEYGMSRAVGSVKLGSGSSEPFVGREMggGSGRDYSENIAETVDAETRALLEAAHDEA 568
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGM--GKRKPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 970471527  569 YQVLNDNRDILDRLAGELLEKETLDAPELVEI 600
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
149-401 3.14e-86

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 274.37  E-value: 3.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  149 MNNKENPQVSFADVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGS 227
Cdd:TIGR01242 111 MEVEERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  228 DFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNR 307
Cdd:TIGR01242 191 ELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNR 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  308 PDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQL 387
Cdd:TIGR01242 271 PDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDY 350
                         250
                  ....*....|....
gi 970471527  388 IDNRALDEAVDRVM 401
Cdd:TIGR01242 351 VTMDDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
159-400 1.24e-80

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 261.00  E-value: 1.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 159 FADVAGSDEAIEELHEI-KEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVG 237
Cdd:COG0464  156 LDDLGGLEEVKEELRELvALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 238 ASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGaGIGGGNDEREqtLNQLLVEMDGFDGktNVILIAATNRPDVLDPALLR 317
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELRS--DVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 318 pgRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDEAV 397
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                 ...
gi 970471527 398 DRV 400
Cdd:COG0464  389 ERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
153-395 1.40e-71

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 245.97  E-value: 1.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  153 ENPQVSFADVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVE 231
Cdd:TIGR01243 446 EVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  232 MFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEReqTLNQLLVEMDGFDGKTNVILIAATNRPDVL 311
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDIL 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  312 DPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNR 391
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683

                  ....
gi 970471527  392 ALDE 395
Cdd:TIGR01243 684 KLEV 687
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
158-327 3.56e-70

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 225.29  E-value: 3.56e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 158 SFADVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGV 236
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 237 GASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALL 316
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 970471527 317 RPGRFDRQIGV 327
Cdd:cd19502  161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
155-382 3.72e-68

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 236.73  E-value: 3.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  155 PQVSFADVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMF 233
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  234 VGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGggnDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDP 313
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDP 329
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970471527  314 ALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTAR 382
Cdd:TIGR01243 330 ALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
149-401 2.63e-63

26S protease regulatory subunit 6B-like protein; Provisional


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 215.01  E-value: 2.63e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 149 MNNKENPQVSFADVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGS 227
Cdd:PTZ00454 134 LQMSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGS 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 228 DFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNR 307
Cdd:PTZ00454 214 EFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNR 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 308 PDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQL 387
Cdd:PTZ00454 294 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYV 373
                        250
                 ....*....|....
gi 970471527 388 IDNRALDEAVDRVM 401
Cdd:PTZ00454 374 ILPKDFEKGYKTVV 387
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
168-325 3.00e-63

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 206.75  E-value: 3.00e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 168 AIEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQ 247
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970471527 248 AKQNAPAIVFIDEIDAVGRHRGAgiGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQI 325
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
159-399 7.50e-63

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 208.97  E-value: 7.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 159 FADVAGSDEAIEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGA 238
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 239 SRVRDLFEQAKQnAPAIVFIDEIDAVGRHRGAGIGGGndEREQTLNQLLVEMDGFDGktNVILIAATNRPDVLDPALLRp 318
Cdd:COG1223   81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 319 gRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDEAVD 398
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                 .
gi 970471527 399 R 399
Cdd:COG1223  234 Q 234
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
149-401 9.81e-63

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 214.63  E-value: 9.81e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 149 MNNKENPQVSFADVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGS 227
Cdd:PTZ00361 172 MKVDKAPLESYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGS 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 228 DFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNR 307
Cdd:PTZ00361 252 ELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNR 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 308 PDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVHAKGKPLAASVDLELLARKTPGFTGADLANVLNEAALLTARSNAQL 387
Cdd:PTZ00361 332 IESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMK 411
                        250
                 ....*....|....
gi 970471527 388 IDNRALDEAVDRVM 401
Cdd:PTZ00361 412 VTQADFRKAKEKVL 425
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
161-325 1.12e-60

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 200.21  E-value: 1.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 161 DVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGAS 239
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 240 RVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGiGGGNDEReqTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPG 319
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREED-QREVERR--VVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                 ....*.
gi 970471527 320 RFDRQI 325
Cdd:cd19503  158 RFDREV 163
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
170-327 8.30e-60

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 197.51  E-value: 8.30e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 170 EELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQA 248
Cdd:cd19511    3 RELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970471527 249 KQNAPAIVFIDEIDAVGRHRGAGIGGGNDEReqTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGV 327
Cdd:cd19511   83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
196-328 1.27e-55

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 185.10  E-value: 1.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  196 VLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGagiGGG 275
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 970471527  276 NDEREQTLNQLLVEMDGFDGKT-NVILIAATNRPDVLDPALLrpGRFDRQIGVD 328
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
170-327 2.71e-55

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 185.41  E-value: 2.71e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 170 EELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQA 248
Cdd:cd19528    3 RELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970471527 249 KQNAPAIVFIDEIDAVGRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGV 327
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
170-327 1.91e-53

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 180.38  E-value: 1.91e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 170 EELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQA 248
Cdd:cd19529    3 QELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970471527 249 KQNAPAIVFIDEIDAVGRHRGAGIGGGNDEReqTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGV 327
Cdd:cd19529   83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
161-325 7.98e-53

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 179.17  E-value: 7.98e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 161 DVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGAS 239
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 240 RVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAgiGGGNDEReQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPG 319
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK--THGEVER-RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*.
gi 970471527 320 RFDRQI 325
Cdd:cd19519  158 RFDREI 163
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
179-327 3.30e-49

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 169.21  E-value: 3.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 179 LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQNAPAIVFI 258
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970471527 259 DEIDAVGRHRGagiGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGV 327
Cdd:cd19530   96 DEVDALVPKRG---DGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
161-325 1.98e-48

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 167.20  E-value: 1.98e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 161 DVAGSDEAIEELHEIKEFLQEPAK-FQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGAS 239
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 240 RVRDLFEQAKQNAPAIVFIDEIDAVGRHRGagiGGGNDEREQTLNQLLVEMDGF----DGKTNVILIAATNRPDVLDPAL 315
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 970471527 316 LRPGRFDRQI 325
Cdd:cd19518  158 RRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
175-325 1.14e-44

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 156.82  E-value: 1.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 175 IKEFLQEPAK----FQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQ 250
Cdd:cd19526    5 LEETIEWPSKypkiFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970471527 251 NAPAIVFIDEIDAVGRHRGAGIGGGNDereQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQI 325
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
174-323 3.34e-40

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 144.58  E-value: 3.34e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 174 EIKEFLQEPAKFQ---AVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFEQAKQ 250
Cdd:cd19527    4 EILDTIQLPLEHPelfSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARD 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970471527 251 NAPAIVFIDEIDAVGRHRGA-GIGGGNDEReqTLNQLLVEMDGF-DGKTNVILIAATNRPDVLDPALLRPGRFDR 323
Cdd:cd19527   84 AKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
162-325 8.33e-40

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 143.65  E-value: 8.33e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 162 VAGSDEAIEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRV 241
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 242 RDLFEQAKQNAPAIVFIDEIDAVGRHRGAgiggGNDEREQTL-NQLLVEMDGFDGKTN--VILIAATNRPDVLDPALLRp 318
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR- 155

                 ....*..
gi 970471527 319 gRFDRQI 325
Cdd:cd19509  156 -RFEKRI 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
161-324 3.81e-39

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 141.88  E-value: 3.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 161 DVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAG-----VPFYSISGSDFVEMFV 234
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 235 GVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAgigggndEREQT----LNQLLVEMDGFDGKTNVILIAATNRPDV 310
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....
gi 970471527 311 LDPALLRPGRFDRQ 324
Cdd:cd19517  154 LDPALRRPGRFDRE 167
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
155-325 9.27e-37

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 135.37  E-value: 9.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 155 PQVSFADVAGSDEAIEELheiKEFLQEPAKFQA--VGAKIP-KGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVE 231
Cdd:cd19521    2 PNVKWEDVAGLEGAKEAL---KEAVILPVKFPHlfTGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 232 MFVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAgigGGNDEREQTLNQLLVEMDGFDGKTNVILI-AATNRPDV 310
Cdd:cd19521   79 KWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVGNDSQGVLVlGATNIPWQ 155
                        170
                 ....*....|....*
gi 970471527 311 LDPALLRpgRFDRQI 325
Cdd:cd19521  156 LDSAIRR--RFEKRI 168
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
154-325 9.28e-32

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 121.63  E-value: 9.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 154 NPQVSFADVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKiPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEM 232
Cdd:cd19525   16 GPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 233 FVGVGASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAgigGGNDEREQTLNQLLVEMDGFDGKTN--VILIAATNRPDV 310
Cdd:cd19525   95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQE 171
                        170
                 ....*....|....*
gi 970471527 311 LDPALLRpgRFDRQI 325
Cdd:cd19525  172 IDEAARR--RLVKRL 184
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
161-321 1.22e-31

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 120.61  E-value: 1.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 161 DVAGSDEAIEELHEIKEF-LQEPAKFQAVG-AKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGA 238
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 239 SRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGigggndEREQTL---NQLLVEMDGF--DGKTNVILIAATNRPDVLDP 313
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST------DHEATAmmkAEFMSLWDGLstDGNCRVIVMGATNRPQDLDE 154
                        170
                 ....*....|
gi 970471527 314 ALLR--PGRF 321
Cdd:cd19520  155 AILRrmPKRF 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
182-325 2.32e-31

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 120.29  E-value: 2.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 182 PAKFQAVGAKIPKGVLLYGPPGTGKTLLARAV-----AGEAGVpfysISGSDFVEMFVGVGASRVRDLFEQAKQNAPA-- 254
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970471527 255 ------IVFIDEIDAVGRHRGAGiGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQI 325
Cdd:cd19504  100 ansglhIIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
169-325 5.10e-31

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 119.32  E-value: 5.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 169 IEELHEIKEFLQE--------PAKFQavGAKIP-KGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGAS 239
Cdd:cd19522    2 IADLEEAKKLLEEavvlpmwmPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 240 RVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAgiGGGNDEREQTLNQLLVEMDGFDGKTN-------VILIAATNRPDVLD 312
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGGASEnddpskmVMVLAATNFPWDID 157
                        170
                 ....*....|...
gi 970471527 313 PALLRpgRFDRQI 325
Cdd:cd19522  158 EALRR--RLEKRI 168
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
186-328 4.32e-29

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 113.01  E-value: 4.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 186 QAVGAKIPKGVLLYGPPGTGKTLLARAVAGEA---GVPFYSISGSDFVEMFVG---VGASRVRDLFEQAKQNAPAIVFID 259
Cdd:cd00009   12 EALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFID 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970471527 260 EIDAVGRhrgagigggnDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGVD 328
Cdd:cd00009   92 EIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
161-327 1.30e-28

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 112.25  E-value: 1.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 161 DVAGSDEAIEELHEIKEF-LQEPAKFQAVGAKiPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGAS 239
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 240 RVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAgigGGNDEREQTLNQLLVEMDGF--DGKTNVILIAATNRPDVLDPALLR 317
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 970471527 318 pgRFDRQIGV 327
Cdd:cd19524  157 --RFTKRVYV 164
ycf46 CHL00195
Ycf46; Provisional
154-376 1.83e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 104.33  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 154 NPQVSFADVAGsdeaieeLHEIKEFLQEPAK-F--QAV--GAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSIsgsD 228
Cdd:CHL00195 222 SVNEKISDIGG-------LDNLKDWLKKRSTsFskQASnyGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---D 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 229 FVEMF---VGVGASRVRDLFEQAKQNAPAIVFIDEID-AVGRHRGAGIGGGNDEREQTLNQLLVEMdgfdgKTNVILIAA 304
Cdd:CHL00195 292 VGKLFggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSEK-----KSPVFVVAT 366
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970471527 305 TNRPDVLDPALLRPGRFDRQIGVDAPSLGGRKQILEVH-AKGKPLA-ASVDLELLARKTPGFTGADLANVLNEA 376
Cdd:CHL00195 367 ANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHlQKFRPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEA 440
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
172-323 5.12e-21

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 90.12  E-value: 5.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 172 LHEIKEFLQEPAK-----FQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFE 246
Cdd:cd19507    5 LDNLKDWLKKRKAafskqASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQ 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970471527 247 QAKQNAPAIVFIDEID-AVGRHRGAGIGGGNderEQTLNQLLVEMDgfDGKTNVILIAATNRPDVLDPALLRPGRFDR 323
Cdd:cd19507   85 TAEAIAPCVLWIDEIEkGFSNADSKGDSGTS---SRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
174-325 6.06e-21

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 89.72  E-value: 6.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 174 EIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDfvemfVGVGASRVRDLFEQAKQNap 253
Cdd:cd19510    4 DLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ-- 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970471527 254 AIVFIDEIDAV---GRHRGAGIGGGNDEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQI 325
Cdd:cd19510   77 SIILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
193-330 4.37e-20

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 87.04  E-value: 4.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527   193 PKGVLLYGPPGTGKTLLARAVAGEA---GVPFYSISGSDFVE--------------MFVGVGASRVRDLFEQAKQNAPAI 255
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970471527   256 VFIDEIDAVGRHRGagigggndEREQTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPgRFDRQIGVDAP 330
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
161-317 5.57e-18

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 81.47  E-value: 5.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 161 DVAGSD---EAIEElhEIKEFLQEPAKFQAVgAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVG 237
Cdd:cd19523    1 DIAGLGalkAAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 238 ASRVRDLFEQAKQNAPAIVFIDEIDAVGRHRGAGIGGGNdeREQTlnQLLVEMDGF--DGKTNVILIAATNRPDVLDPAL 315
Cdd:cd19523   78 EKILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG--RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESL 153

                 ..
gi 970471527 316 LR 317
Cdd:cd19523  154 RR 155
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
186-305 8.33e-14

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 73.97  E-value: 8.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 186 QAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFvemfvgvGASRVRDLFEQAKQNAPA----IVFIDEI 261
Cdd:PRK13342  29 RMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRSAgrrtILFIDEI 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 970471527 262 davgrHRgagigggndereqtLN---Q--LL--VEmdgfDGKtnVILIAAT 305
Cdd:PRK13342 102 -----HR--------------FNkaqQdaLLphVE----DGT--ITLIGAT 127
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
186-399 2.25e-13

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 72.78  E-value: 2.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 186 QAVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGsdfvemfVGVGASRVRDLFEQAKQNA----PAIVFIDEI 261
Cdd:COG2256   42 RAIEAGRLSSMILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 262 davgrHRgagigggndereqtLN---Q--LL--VEmDGfdgktNVILIAAT--NrPD-VLDPAL--------LRP----- 318
Cdd:COG2256  115 -----HR--------------FNkaqQdaLLphVE-DG-----TITLIGATteN-PSfEVNSALlsrcrvfvLKPlseed 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 319 --GRFDRQIGVDAPSLGGRKQILEVHAkgkplaasvdLELLARktpgFTGADLANVLN---EAALLTARSNAQLIDNRAL 393
Cdd:COG2256  169 leQLLERALADDERGLGGYKLELDDEA----------LEALAR----LADGDARRALNaleLAVLSAPPDGVIEITLELV 234

                 ....*.
gi 970471527 394 DEAVDR 399
Cdd:COG2256  235 EEALQR 240
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
194-315 2.30e-13

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 67.94  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 194 KGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGvGASRVRDLFEQA-KQNAPAIVFIDEIDAVGRHRgAGI 272
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKR-STE 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 970471527 273 GGGNDEReQTLNQLLVEMDgfDGKTNVILIAATNRPDVLDPAL 315
Cdd:cd19512  101 KISEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI 140
PRK04195 PRK04195
replication factor C large subunit; Provisional
158-277 1.15e-12

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 70.72  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 158 SFADVAGSDEAIEELHE-IKEFLQEpakfqavgaKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDF-----VE 231
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREwIESWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 970471527 232 MFVGvGASRVRDLFEQAKQnapaIVFIDEIDavgrhrgaGIGGGND 277
Cdd:PRK04195  83 RVAG-EAATSGSLFGARRK----LILLDEVD--------GIHGNED 115
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
193-327 4.78e-11

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 61.62  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 193 PKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFV--------------EMFVGVGASRVRDLFEQAKQNAPAIVFI 258
Cdd:cd19505   12 SKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSPCIIWI 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970471527 259 DEIDAVGRHRgagigGGNDEREQT------LNQLLVEMDGFDGKTNVILIAATNRPDVLDPALLRPGRFDRQIGV 327
Cdd:cd19505   92 PNIHELNVNR-----STQNLEEDPklllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
192-321 7.22e-11

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 61.63  E-value: 7.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 192 IPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEM-FVGVGA-SRVRDLFEqakqnapAIVFIDEIDAVGRHrg 269
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVE-------GIVFIDEIDKIAKR-- 115
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970471527 270 AGIGGGNDEREQTLNQLL-------VEMDGFDGKTNVILIAATNRPDVLDPALLRP---GRF 321
Cdd:cd19498  116 GGSSGPDVSREGVQRDLLpivegstVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPelqGRF 177
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
351-395 7.40e-10

AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 54.47  E-value: 7.40e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 970471527  351 SVDLELLARKTPGFTGADLANVLNEAALLTARSNAQLIDNRALDE 395
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
196-268 2.19e-07

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 53.21  E-value: 2.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970471527 196 VLLYGPPGTGKTLLARAVAGEAGVPFYSISG------SDFVEMFVGVGAsrvRDlfeqakqnapaIVFIDEIdavgrHR 268
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI-----HR 113
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
195-321 2.69e-07

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.98  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  195 GVLLYGPPGTGKTLLARAVAgEA--GVPFYSISGSDF---------VEMFVGVGASRVRDLFEQAKQnaPAIVFIDEIDA 263
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteedlfgrRNIDPGGASWVDGPLVRAARE--GEIAVLDEINR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970471527  264 vgrhrgagiggGNDEREQTLNQLLVE-----MDGF----DGKTNVILIAATNRPD----VLDPALLRpgRF 321
Cdd:pfam07728  78 -----------ANPDVLNSLLSLLDErrlllPDGGelvkAAPDGFRLIATMNPLDrglnELSPALRS--RF 135
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
193-440 9.37e-07

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 51.39  E-value: 9.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 193 PKGVLLYGPPGTGKTLLARAV-------AGEAGVPF-------------YSI---------SGSDFVEmfVGVGASRVRD 243
Cdd:COG1474   51 PSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVrvvyvncrqastrYRVlsrileelgSGEDIPS--TGLSTDELFD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 244 LFEQA--KQNAPAIVFIDEIDAVGRhrgagigggnDEREQTLNQLLVEMDGFDG-KTNVILIaaTNRPDV---LDPAL-- 315
Cdd:COG1474  129 RLYEAldERDGVLVVVLDEIDYLVD----------DEGDDLLYQLLRANEELEGaRVGVIGI--SNDLEFlenLDPRVks 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 316 -LRPG--RFDRqigVDAPSLggrKQILEVHAK----GKPLAASVdLELLARKTPGFTG-ADLA-NVLNEAALLTARSNAQ 386
Cdd:COG1474  197 sLGEEeiVFPP---YDADEL---RDILEDRAElafyDGVLSDEV-IPLIAALAAQEHGdARKAiDLLRVAGEIAEREGSD 269
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 970471527 387 LIDNRALDEAVDRVMAGpQRRTRI--MSDQEKLItayhegGHALAAAAMRHTDPVT 440
Cdd:COG1474  270 RVTEEHVREAREKIERD-RLLEVLrgLPTHEKLV------LLAIAELLKDGEDPVR 318
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
194-229 9.96e-07

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 51.51  E-value: 9.96e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 970471527 194 KGVLLYGPPGTGKTLLARAVAGEAG--VPFYSISGSDF 229
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
196-312 1.03e-06

RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 47.88  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 196 VLLYGPPGTGKTLLARAVAGEA---GVPFYSISgsdFVEMFVgvgaSRVRDLFEQAKqnaPAIVFIDEIDAVGRHRgagi 272
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARAS---- 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 970471527 273 ggGNDEREQTLNQLLVEMDGFdGKTNVILIAATNRPDVLD 312
Cdd:cd01120   67 --QGDRSSELLEDLAKLLRAA-RNTGITVIATIHSDKFDI 103
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
172-269 1.36e-06

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 49.09  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 172 LHEIKEFLQEpakFQAVGA--KIPKG--VLLYGPPGTGKTLLARAVAGEAGVPFYSIS-G--SDFVEM------FVGVGA 238
Cdd:cd19500   15 LEDVKERILE---YLAVRKlkGSMKGpiLCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghrrtYVGAMP 91
                         90       100       110
                 ....*....|....*....|....*....|..
gi 970471527 239 SRVRDLFEQAKQNAPAIVfIDEIDAVGR-HRG 269
Cdd:cd19500   92 GRIIQALKKAGTNNPVFL-LDEIDKIGSsFRG 122
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
196-315 1.61e-06

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 49.37  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 196 VLLYGPPGTGKTLLARAVAGEAGV---------------------PFYSISGSDFVEMFvgvgaSRVRDLFEQakQNAPA 254
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIrlssryrygqlieinshslfsKWFSESGKLVTKMF-----QKIQELIDD--KDALV 127
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970471527 255 IVFIDEIDAVGRHRGAgIGGGNDERE--QTLNQLLVEMDGFDGKTNVILIAATNRPDVLDPAL 315
Cdd:cd19508  128 FVLIDEVESLAAARSA-SSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
157-261 3.05e-06

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 50.15  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 157 VSFADVAGSDEAIEELHEIKEFLQE--PAKFQAVGA--KIPKGVLLYGPPGTGKTLLARAVAGEAG---------VPFY- 222
Cdd:COG1401  181 LSAAEELYSEDLESEDDYLKDLLREkfEETLEAFLAalKTKKNVILAGPPGTGKTYLARRLAEALGgedngriefVQFHp 260
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 970471527 223 SISGSDFVEMFVGVGAS---RVRD-LF----EQAKQN--APAIVFIDEI 261
Cdd:COG1401  261 SWSYEDFLLGYRPSLDEgkyEPTPgIFlrfcLKAEKNpdKPYVLIIDEI 309
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
194-229 3.16e-06

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 49.62  E-value: 3.16e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 970471527  194 KGVLLYGPPGTGKTLLARAVAGEAG--VPFYSISGSDF 229
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
196-226 3.28e-06

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 47.49  E-value: 3.28e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 970471527  196 VLLYGPPGTGKTLLARAVAGEAGVPFYSISG 226
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
164-325 7.84e-06

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 49.07  E-value: 7.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  164 GSDEAIEELHEIKEFLQEPAKFQAVGAKIP---KGVLLYGPPGTGKTLLARAVAGE-AGVPFYS------ISGSDFVEMF 233
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  234 VGVGASRVRDLFEQAkqnAPAIVFIDEIDA-VGRHRGAgiggGNDEREQTLNQLLVEMDgfDGKTNVILIAATNRPDvLD 312
Cdd:TIGR03922 360 IGESEAKTNEIIDSA---LGGVLFLDEAYTlVETGYGQ----KDPFGLEAIDTLLARME--NDRDRLVVIGAGYRKD-LD 429
                         170
                  ....*....|....*...
gi 970471527  313 PAL-----LRpGRFDRQI 325
Cdd:TIGR03922 430 KFLevnegLR-SRFTRVI 446
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
196-461 1.07e-05

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 47.85  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 196 VLLYGPPGTGKTLLARAVAGEAGVPFYSISG------------SDFVEMFvgvGASRVRD--LFEQakqnapaIVFIDEI 261
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllpsdilgtYIYDQQT---GEFEFRPgpLFAN-------VLLADEI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 262 DavgrhRGagigggndeREQTLNQLLVEMDGF----DGKT-----NVILIAATNRPDV-----LDPALLRpgRFDRQIGV 327
Cdd:COG0714  104 N-----RA---------PPKTQSALLEAMEERqvtiPGGTyklpePFLVIATQNPIEQegtypLPEAQLD--RFLLKLYI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 328 DAPSLGGRKQILEVHAKGKPlaasvdlellarktpgftgADLANVLNEAALLTARsnaQLIDNRALDEAVDRVMAGPQRR 407
Cdd:COG0714  168 GYPDAEEEREILRRHTGRHL-------------------AEVEPVLSPEELLALQ---ELVRQVHVSEAVLDYIVDLVRA 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970471527 408 TRIMSDQEK---------LITAyhegghALAAAAMRHTDPVTKITILP-RGRALGYTMVLPLED 461
Cdd:COG0714  226 TREHPDLRKgpsprasiaLLRA------ARALALLDGRDYVTPDDVKAvAGPVLKHRLILSPEA 283
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
11-104 1.24e-05

FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only membrane-bound ATP-dependent protease universally conserved in prokaryotes. It only efficiently degrades proteins that have a low thermodynamic stability - e.g. it lacks robust unfoldase activity. This feature may be key and implies that this could be a criterion for degrading a protein. In Oenococcus oeni FtsH is involved in protection against environmental stress, and shows increased expression under heat or osmotic stress. These two lines of evidence suggest that it is a fundamental prokaryotic self-protection mechanism that checks if proteins are correctly folded (personal obs: Yeats C). The precise function of this N-terminal region is unclear.


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 44.52  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527   11 YLYVLIALVGIFIGWSVIAQSGTQQIDTQKGLEQLADGKVSSVVVNSTEQR----VDLTLKDGNAKEQFYY-STPRGEEV 85
Cdd:pfam06480   4 WLLILLVLLLLFLLFLLSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDEILptgvVEGTLKDGSKFTTYFIpSLPNVDSL 83
                          90
                  ....*....|....*....
gi 970471527   86 IKAVNDANLPDGYNDTVQQ 104
Cdd:pfam06480  84 LEKLEDALEEKGVKVSVKP 102
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
196-226 1.96e-05

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 47.00  E-value: 1.96e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 970471527 196 VLLYGPPGTGKTLLARAVAGEAGVPFYSISG 226
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
196-266 2.18e-05

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 46.91  E-value: 2.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970471527  196 VLLYGPPGTGKTLLARAVAGEAGVPFYSISG------SDFVEMFVGVGAsrvRDlfeqakqnapaIVFIDEIDAVGR 266
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEIHRLSP 95
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
172-263 3.86e-05

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 46.12  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 172 LHEIKEFLQEPAKfqavGAKIPKGVLLYGPPGTGKTLLARAVAGE---------------AGVPFYSISGSDFVEMFVGV 236
Cdd:COG0470    1 QEEAWEQLLAAAE----SGRLPHALLLHGPPGIGKTTLALALARDllcenpeggkacgqcHSRLMAAGNHPDLLELNPEE 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 970471527 237 -----GASRVRDLFEQAKQNAPA----IVFIDEIDA 263
Cdd:COG0470   77 ksdqiGIDQIRELGEFLSLTPLEggrkVVIIDEADA 112
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
193-262 6.17e-05

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.11  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  193 PKGV-LLYGPPGTGKTLLARAVAGEAGV---PFYSISGSDFVE-----MFVG-----VGASRVRDLFEQAKQNAPAIVFI 258
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81

                  ....
gi 970471527  259 DEID 262
Cdd:pfam07724  82 DEIE 85
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
173-266 6.85e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.53  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 173 HEIKEFL------QEPAKFQ---AV---------GAKIPKGV-------LLYGPPGTGKTLLARAVAGEAGVPFySIS-- 225
Cdd:PRK05342  63 KEIKAHLdqyvigQERAKKVlsvAVynhykrlrhGDKKDDDVelqksniLLIGPTGSGKTLLAQTLARILDVPF-AIAda 141
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 970471527 226 ---------GSDfVEMFVgvgasrVRDLF------EQAKQnapAIVFIDEIDAVGR 266
Cdd:PRK05342 142 ttlteagyvGED-VENIL------LKLLQaadydvEKAQR---GIVYIDEIDKIAR 187
PRK13341 PRK13341
AAA family ATPase;
197-268 6.98e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.20  E-value: 6.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970471527 197 LLYGPPGTGKTLLARAVAGEAGVPFYSISGsdfvemfVGVGASRVRDLFEQAKQ-----NAPAIVFIDEIdavgrHR 268
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKErlerhGKRTILFIDEV-----HR 120
44 PHA02544
clamp loader, small subunit; Provisional
191-265 7.04e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 45.37  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 191 KIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDfvemfvgvgaSRVRDLFEQAKQNA--------PAIVFIDEID 262
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD----------CRIDFVRNRLTRFAstvsltggGKVIIIDEFD 110

                 ...
gi 970471527 263 AVG 265
Cdd:PHA02544 111 RLG 113
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
173-266 7.21e-05

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 44.90  E-value: 7.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 173 HEIKEFL------QEPAK-FQAV------------------GAKIPKG-VLLYGPPGTGKTLLARAVAGEAGVPFYSISG 226
Cdd:cd19497    4 KEIKEHLdkyvigQERAKkVLSVavynhykrirnnlkqkddDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIADA 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 970471527 227 SDFVEM-FVGvgaSRVRDLFEQAKQNA--------PAIVFIDEIDAVGR 266
Cdd:cd19497   84 TTLTEAgYVG---EDVENILLKLLQAAdydveraqRGIVYIDEIDKIAR 129
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
173-266 7.62e-05

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 45.42  E-value: 7.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 173 HEIKEFL------QEPAK--------------FQAVGAK----IPKG-VLLYGPPGTGKTLLARAVAGEAGVPFySIS-- 225
Cdd:COG1219   64 KEIKAFLdeyvigQERAKkvlsvavynhykrlNSGSKDDddveLEKSnILLIGPTGSGKTLLAQTLARILDVPF-AIAda 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 970471527 226 ---------GSDfVEMFVgvgasrVR-------DLfEQAKQnapAIVFIDEIDAVGR 266
Cdd:COG1219  143 ttlteagyvGED-VENIL------LKllqaadyDV-EKAER---GIIYIDEIDKIAR 188
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
192-332 1.26e-04

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 45.08  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 192 IPKGVLLYGPPGTGKTLLARAVA----GEAG------VPFY-SISGSDFVEMFV--GVGASRVRDLF----EQAKQNaPA 254
Cdd:PRK11331 193 IKKNIILQGPPGVGKTFVARRLAylltGEKApqrvnmVQFHqSYSYEDFIQGYRpnGVGFRRKDGIFynfcQQAKEQ-PE 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 255 IVFIDEIDAVGRHRGAGIGG------GNDEREQTLNQLLV----EMDGFDGKTNVILIAATNRPD----VLDPALLRPGR 320
Cdd:PRK11331 272 KKYVFIIDEINRANLSKVFGevmmlmEHDKRGENWSVPLTysenDEERFYVPENVYIIGLMNTADrslaVVDYALRRRFS 351
                        170
                 ....*....|...
gi 970471527 321 F-DRQIGVDAPSL 332
Cdd:PRK11331 352 FiDIEPGFDTPQF 364
AAA_22 pfam13401
AAA domain;
196-311 1.27e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 42.33  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  196 VLLYGPPGTGKTLLARAVA---GEAGVPFYSI------SGSDFVEMFV---------GVGASRVRDLFEQA--KQNAPAI 255
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVdlpsgtSPKDLLRALLralglplsgRLSKEELLAALQQLllALAVAVV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 970471527  256 VFIDEIDAVgrhrgagigggndeREQTLNQLLVEMDGFDGKTNVILIAATNRPDVL 311
Cdd:pfam13401  88 LIIDEAQHL--------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
162-262 3.08e-04

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.16  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 162 VAGSDEAIEELHEI----KEFLQEPAKfqavgakiPKGVLLY-GPPGTGKTLLARAVAGE---AGVPFYSISGSDFVEMF 233
Cdd:cd19499   13 VVGQDEAVKAVSDAirraRAGLSDPNR--------PIGSFLFlGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKH 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 970471527 234 VG----------VGASRVRDLFEQAKQNAPAIVFIDEID 262
Cdd:cd19499   85 SVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
PRK12422 PRK12422
chromosomal replication initiator protein DnaA;
154-344 3.50e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 183521 [Multi-domain]  Cd Length: 445  Bit Score: 43.67  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 154 NPQVSFADVAGSDEAIEElHEIkefLQEPAKFQAVGAKIP-KGVLLYGPPGTGKTLLARAVAG---EAGVPFYSISGSDF 229
Cdd:PRK12422 105 DPLMTFANFLVTPENDLP-HRI---LQEFTKVSEQGKGFPfNPIYLFGPEGSGKTHLMQAAVHalrESGGKILYVRSELF 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 230 VEMFVGVGASRVRDLFEQAKQNAPAIvFIDEIdavgrHRGAGIGGGNDEREQTLNQLLVEmdgfdGKtnVILIAATNRPD 309
Cdd:PRK12422 181 TEHLVSAIRSGEMQRFRQFYRNVDAL-FIEDI-----EVFSGKGATQEEFFHTFNSLHTE-----GK--LIVISSTCAPQ 247
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 970471527 310 VL---DPALLrpGRFDRQIGVDAPSL--GGRKQILEVHAK 344
Cdd:PRK12422 248 DLkamEERLI--SRFEWGIAIPLHPLtkEGLRSFLERKAE 285
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
196-306 3.84e-04

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 40.28  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  196 VLLYGPPGTGKTL----LARAVAGEAGVP---FYSI-SGSDFVEMFVGvgasrvrdlfeqakqnaPAIVFIDEIDAVgrh 267
Cdd:pfam00910   1 IWLYGPPGCGKSTlakyLARALLKKLGLPkdsVYSRnPDDDFWDGYTG-----------------QPVVIIDDFGQN--- 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 970471527  268 rgagiggGNDEREQTLNQLL------VEMDGFDGK----TNVILIAATN 306
Cdd:pfam00910  61 -------PDGPDEAELIRLVsstpypPPMAALEEKgtpfTSKFVIVTSN 102
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
162-257 4.42e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 41.34  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  162 VAGSDEAIEELHEIkeflqepakFQAVGAKIPKGVLLYGPPGTGKTLLARAV---AGEAGVPFYSISGSDFVEMFVGVGA 238
Cdd:pfam13191   2 LVGREEELEQLLDA---------LDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLLEA 72
                          90
                  ....*....|....*....
gi 970471527  239 SRVRDLFEQAKQNAPAIVF 257
Cdd:pfam13191  73 LTREGLLRQLLDELESSLL 91
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
164-267 4.48e-04

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 43.01  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  164 GSDEAIEELheiKEFLQEpakfqAVGAKIPKGVLLYGPPGTGKTLLARAV-------AGEAGVPF---------YSISGS 227
Cdd:TIGR02928  19 HRDEQIEEL---AKALRP-----ILRGSRPSNVFIYGKTGTGKTAVTKYVmkeleeaAEDRDVRVvtvyvncqiLDTLYQ 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 970471527  228 DFVEMF------------VGVGASRV-RDLFEQAKQNAPAIVFI-DEIDAVGRH 267
Cdd:TIGR02928  91 VLVELAnqlrgsgeevptTGLSTSEVfRRLYKELNERGDSLIIVlDEIDYLVGD 144
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
182-308 4.63e-04

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 41.36  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 182 PAKFQAVGAKIP--KGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASR--VRDLFEQAKQNAPAIVF 257
Cdd:cd19506   13 PLGSQAVHEKAPlvKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIW 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 970471527 258 IDEIDAVGRHRGAGIGGGNDER--EQTLNQLLVEMDGFDgktNVILIAATNRP 308
Cdd:cd19506   93 IGDAEKTFYKKVPKTEKQLDPKrlKKDLPKILKSLKPED---RVLIVGTTSRP 142
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
196-416 8.16e-04

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 42.10  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 196 VLLYGPPGTGKTLLARAVAGEAGVPFYS-----ISGSDFVEMFvgVGASRVRDLFE-QAKQNAPAIVFIDEIdavgrHRG 269
Cdd:COG0593   37 LFLYGGVGLGKTHLLHAIGNEALENNPGarvvyLTAEEFTNDF--INAIRNNTIEEfKEKYRSVDVLLIDDI-----QFL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 270 AGigggnDEREQ-----TLNQLLvemdgFDGKTnvILIAATNRP---DVLDPALLRpgRFDR--QIGVDAPSLGGRKQIL 339
Cdd:COG0593  110 AG-----KEATQeeffhTFNALR-----EAGKQ--IVLTSDRPPkelPGLEERLRS--RLEWglVVDIQPPDLETRIAIL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 340 EVHAKGKPLAASVD-LELLARKTPGfTGADLanvlnEAAL--LTARSNAQlidNRALD-----EAVDRVMAGPQRRTRIM 411
Cdd:COG0593  176 RKKAADRGLELPDEvLEYLARRIER-NVREL-----EGALnrLDAYALLT---GRPITlelarEVLKDLLRAQKKEITIE 246

                 ....*
gi 970471527 412 SDQEK 416
Cdd:COG0593  247 DIQKA 251
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
158-262 9.45e-04

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 42.19  E-value: 9.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 158 SFADVAGSDEAIEELHEIkeflqepAKfQAVGAKIPkgVLLYGPPGTGKTLLARAVAGE---AGVPFY-----SISGSDF 229
Cdd:COG3284  319 ALAALAGGDPAMRRALRR-------AR-RLADRDIP--VLILGETGTGKELFARAIHAAsprADGPFVavncaAIPEELI 388
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 970471527 230 V-EMFVGV-----GASRV--RDLFEQAkqnAPAIVFIDEID 262
Cdd:COG3284  389 EsELFGYEpgaftGARRKgrPGKIEQA---DGGTLFLDEIG 426
PRK08939 PRK08939
primosomal protein DnaI; Reviewed
156-216 9.51e-04

primosomal protein DnaI; Reviewed


Pssm-ID: 236353 [Multi-domain]  Cd Length: 306  Bit Score: 41.78  E-value: 9.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970471527 156 QVSFADVAGSDEA-IEELHEIKEFLQE--PAKFQavgakipKGVLLYGPPGTGKTLLARAVAGE 216
Cdd:PRK08939 123 QASLADIDLDDRDrLDALMAALDFLEAypPGEKV-------KGLYLYGDFGVGKSYLLAAIANE 179
rfc PRK00440
replication factor C small subunit; Reviewed
152-263 1.39e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 41.40  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 152 KENPQvSFADVAGSDEAIEELheiKEFlqepakfqaVGAK-IPKgVLLYGPPGTGKTLLARAVAGEagvpfysISGSDFV 230
Cdd:PRK00440  10 KYRPR-TLDEIVGQEEIVERL---KSY---------VKEKnMPH-LLFAGPPGTGKTTAALALARE-------LYGEDWR 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 970471527 231 EMFVGVGAS----------RVRDlFEQAKQNAPA---IVFIDEIDA 263
Cdd:PRK00440  69 ENFLELNASdergidvirnKIKE-FARTAPVGGApfkIIFLDEADN 113
Sigma54_activat pfam00158
Sigma-54 interaction domain;
190-261 2.41e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 39.31  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527  190 AKIPKGVLLYGPPGTGKTLLARAV---AGEAGVPFYSISGSDFV------EMFvGV------GASRVRD-LFEQAKQnap 253
Cdd:pfam00158  19 APTDAPVLITGESGTGKELFARAIhqlSPRADGPFVAVNCAAIPeellesELF-GHekgaftGADSDRKgLFELADG--- 94

                  ....*...
gi 970471527  254 AIVFIDEI 261
Cdd:pfam00158  95 GTLFLDEI 102
PRK08116 PRK08116
hypothetical protein; Validated
195-216 3.23e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.00  E-value: 3.23e-03
                         10        20
                 ....*....|....*....|..
gi 970471527 195 GVLLYGPPGTGKTLLARAVAGE 216
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANE 137
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
158-249 3.26e-03

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 40.36  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 158 SFADVAGSDEAIEELHEikeflqepakfqAVGAKIPKGVLLYGPPGTGKTLLARAVAGEA-GVPFysisGSDFVEMfvgv 236
Cdd:PRK12402  13 LLEDILGQDEVVERLSR------------AVDSPNLPHLLVQGPPGSGKTAAVRALARELyGDPW----ENNFTEF---- 72
                         90
                 ....*....|...
gi 970471527 237 gasRVRDLFEQAK 249
Cdd:PRK12402  73 ---NVADFFDQGK 82
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
194-261 3.98e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.38  E-value: 3.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970471527 194 KGVLLYGPPGTGKTLLARAVAGEA---GVPFYSISGSDFV-EMFVGVGASRVRDLFEQAKQnaPAIVFIDEI 261
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRFTTAPDLVnELKEARADGRLERLLKRLAK--VDLLILDEL 169
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
196-222 5.00e-03

Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses encode two non-structural proteins, NS1 and NS2. The mRNA for NS2 contains the coding sequence for the first 87 amino acids of NS1, then by an alternative splicing mechanism mRNA from a different reading frame, encoding the last 78 amino acids, makes up the full length of the NS2 mRNA. NS1, is the major non-structural protein. It is essential for DNA replication. It is an 83-kDa nuclear phosphoprotein. It has DNA helicase and ATPase activity.


Pssm-ID: 426020  Cd Length: 271  Bit Score: 39.21  E-value: 5.00e-03
                          10        20
                  ....*....|....*....|....*..
gi 970471527  196 VLLYGPPGTGKTLLARAVAgeAGVPFY 222
Cdd:pfam01057 116 VWFYGPASTGKTNLAQAIA--HAVPLY 140
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
172-269 5.25e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 40.00  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 172 LHEIK----EFLqepakfqAVGAKIPKG----VLLYGPPGTGKTLLARAVAgEA-GVPFYSISgsdfvemfVGvGasrVR 242
Cdd:COG0466  330 LEKVKerilEYL-------AVRKLKKKLkgpiLCLVGPPGVGKTSLGKSIA-RAlGRKFVRIS--------LG-G---VR 389
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 970471527 243 DlfE-----------------------QAKQNAPaiVFI-DEIDAVGR-HRG 269
Cdd:COG0466  390 D--EaeirghrrtyigampgriiqglkKAGTKNP--VFLlDEIDKMGSdFRG 437
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
196-490 6.57e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.79  E-value: 6.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 196 VLLYGPPGTGKTLLARAVA---------GEAGVPFY--------SISGSDFVEMFVGVGASRVRDLFEQAKQNAPAIVFI 258
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrdlaeEASLEDLLAEALEKRGGEPEDALERLLRNGRLLLLL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 259 DEIDAVGRHrgagigggnDEREQTLNQLLVEMDGFDgKTNVILiaaTNRPDVLDPALLRPGR------FDR-QIgvdaps 331
Cdd:COG5635  263 DGLDEVPDE---------ADRDEVLNQLRRFLERYP-KARVII---TSRPEGYDSSELEGFEvlelapLSDeQI------ 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 332 lggrKQILEVHAKGKPLAASVDLELLARkTPGFtgADLAN--VLNEAALLTARSNAQLIDNRA--LDEAVDRVMagpQRR 407
Cdd:COG5635  324 ----EEFLKKWFEATERKAERLLEALEE-NPEL--RELARnpLLLTLLALLLRERGELPDTRAelYEQFVELLL---ERW 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970471527 408 trimsDQEKLITAYHEGGHALAAAAMRHtdpvtkitilprgraLGYTMVlpLEDKYSVTRNELLDQLTYAMGGRVAEEIV 487
Cdd:COG5635  394 -----DEQRGLTIYRELSREELRELLSE---------------LALAMQ--ENGRTEFAREELEEILREYLGRRKDAEAL 451

                 ...
gi 970471527 488 FHD 490
Cdd:COG5635  452 LDE 454
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
196-215 6.90e-03

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 39.25  E-value: 6.90e-03
                         10        20
                 ....*....|....*....|
gi 970471527 196 VLLYGPPGTGKTLLARAVAG 215
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
196-215 7.47e-03

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.29  E-value: 7.47e-03
                          10        20
                  ....*....|....*....|
gi 970471527  196 VLLYGPPGTGKTLLARAVAG 215
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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